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GSIC_ECOL6
ID   GSIC_ECOL6              Reviewed;         306 AA.
AC   Q8FJK9;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Glutathione transport system permease protein GsiC {ECO:0000250|UniProtKB:P75798};
GN   Name=gsiC {ECO:0000250|UniProtKB:P75798}; OrderedLocusNames=c0916;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- FUNCTION: Part of the ABC transporter complex GsiABCD involved in
CC       glutathione import. Probably responsible for the translocation of the
CC       substrate across the membrane. {ECO:0000250|UniProtKB:P75798}.
CC   -!- SUBUNIT: The complex is composed of two ATP-binding proteins (GsiA),
CC       two transmembrane proteins (GsiC and GsiD) and a solute-binding protein
CC       (GsiB). {ECO:0000250|UniProtKB:P75798}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000250|UniProtKB:P75798}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC       permease family. {ECO:0000305}.
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DR   EMBL; AE014075; AAN79389.1; -; Genomic_DNA.
DR   RefSeq; WP_000936053.1; NC_004431.1.
DR   AlphaFoldDB; Q8FJK9; -.
DR   SMR; Q8FJK9; -.
DR   STRING; 199310.c0916; -.
DR   EnsemblBacteria; AAN79389; AAN79389; c0916.
DR   KEGG; ecc:c0916; -.
DR   eggNOG; COG0601; Bacteria.
DR   HOGENOM; CLU_036879_0_0_6; -.
DR   OMA; MQEDYMR; -.
DR   BioCyc; ECOL199310:C0916-MON; -.
DR   Proteomes; UP000001410; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR   CDD; cd06261; TM_PBP2; 1.
DR   Gene3D; 1.10.3720.10; -; 1.
DR   InterPro; IPR045621; BPD_transp_1_N.
DR   InterPro; IPR000515; MetI-like.
DR   InterPro; IPR035906; MetI-like_sf.
DR   Pfam; PF00528; BPD_transp_1; 1.
DR   Pfam; PF19300; BPD_transp_1_N; 1.
DR   SUPFAM; SSF161098; SSF161098; 1.
DR   PROSITE; PS50928; ABC_TM1; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Membrane; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..306
FT                   /note="Glutathione transport system permease protein GsiC"
FT                   /id="PRO_0000279991"
FT   TOPO_DOM        1..8
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        9..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        30..102
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        103..123
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        124..134
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        135..155
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        156..168
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        169..189
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        190..228
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        229..249
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        250..277
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        278..298
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        299..306
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          95..292
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
SQ   SEQUENCE   306 AA;  34032 MW;  52DC82A3D6EB2406 CRC64;
     MLNYVIKRLL GLIPTLFIVS VLVFLFVHML PGDPARLIAG PEADAQVIEL VRQQLGLDQP
     LYHQFWHYIS NAVQGDLGLS MVSRRPVADE IASRFMPTLW LTITSMVWAV IFGMAAGIIA
     AVWRNRWPDR LSMTIAVSGI SFPAFALGML LIQVFSVELG WLPTVGADSW QHYILPSLTL
     GAAVAAVMAR FTRASFVDVL SEDYMRTARA KGVSETWVVL KHGLRNAMIP VVTMMGLQFG
     FLLGGSIVVE KVFNWPGLGR LLVDSVEMRD YPVIQAEILL FSLEFILINL VVDVLYAAIN
     PAIRYK
 
 
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